The emerging prevalence of bacteria resistant to common therapeutic agents has led to a dire need for new antimicrobial compounds.1 Peptide antimicrobials,2 a central element of the human immune system, have received increasing interest as potentially new antimicrobial treatments. One reason for their potential success is that it appears to be difficult, although not impossible, for pathogenic microbes to develop resistance to these innate “host-defense” peptides. One large subset of host-defense peptides forms an amphiphilic α-helical structure. These peptides act by disrupting bacterial membranes because their net positive charge attracts the peptides to the negatively charged bacterial membrane,4 and the hydrophobic face of the helix allows the formation of aggregates that compromise membrane integrity.2 Amphiphilic topology also plays a factor in the biological activity of these molecules, as enantiomeric peptides retain full activity.5 
This design principle has been applied to distinct types of amphiphilic helical antimicrobial oligomers. For example, β-Amino acid oligomers (“β-peptides”) can adopt discrete helical conformations.6 By properly arranging cationic and lipophilic residues within the β-peptide, amphiphilic helices with antimicrobial activity can by obtained.7-9 DeGrado et al. also describe aryl amide oligomers with elongated conformations that can project lipophilic and cationic groups to opposite sides of the molecular backbone.10 Unlike α- or β-peptide oligomers, these aryl amide oligomers are achiral.